• International Journal of Industrial Entomology and Biomaterials
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• v.37 no.1
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• pp.29-32
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• 2018

Silkworm powder's thermal property is an important factor for its storage and marketing. This study examined the effect of edible enzyme on the thermal property of silkworm powder using Thermogravimetric Analysis (TGA) and Differential Scanning Calorimetry (DSC). Results of the TGA showed that regardless of the enzyme treatment, the weight loss patterns of silkworm powders exhibited 3 step thermal property deterioration at approximately $80^{\circ}C$, $280^{\circ}C$, and $480^{\circ}C$ due to water evaporation and thermal degradation. This is similar with the DSC which also resulted in all samples two endothermic peaks attributed also to water evaporation and thermal degradation. These results indicated that the use of enzyme such as protease and cellulase might not affect significantly the thermal properties of silkworm powder.

• Korean Chemical Engineering Research
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• v.54 no.5
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• pp.665-670
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• 2016

This study deals with the possible degradation of toluene and acetic acid when subjected to cell-free enzyme system from the toluene degrading bacteria Pseudomonas putida and acetic acid degrading bacteria Cupriavidus necator. P. putida produces toluene dioxygenase only under the existence of toluene in culture medium and toluene is degraded to cis-toluene dihydrodiol by this enzyme. C. necator produces acetyl coenzyme A synthetase-1 and converts acetic acid to acetyl CoA in order to synthesize ATP to need for growth or PHA which is biodegradable polymer. In case of toluene degradation, the experiment was conducted before and after production of toluene dioxygenase as this enzyme, produced by P. putida, is an inducible enzyme. Toluene was detected using gas chromatography (GC). Similar amount of toluene was found in control group and before production of toluene dioxygenase (experimental group 1). However, reduction in toluene was detected after the production of toluene dioxygenase (experimental group 2). Acetic acid was detected through application of gas chromatography-mass spectrometer (GC-MS). The results showed the acetic acid peak was not detected in the experimental group to apply cell-free enzyme system. These results show that the cell-free enzyme system obtained from P. putida and C. necator retained the ability to degrade toluene and acetic acid. However, P. putida needs to produce the inducible enzyme before preparation of the cell-free enzyme system.

• Journal of the Korean Wood Science and Technology
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• v.27 no.4
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• pp.1-14
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• 1999

As the biodegradation of wood constituents has been understood as a multi-basidiomycetes and enzymatic processes, this review will focus on the roles of low molecular compounds and radicals working in harmony with fungal enzymes. Wood rotting basidiomycete fungi penetrate wood, and lead to more easily metabolize carbohydrates of the wood complex. The white-rot fungi, having versatile enzymes, are able to attack directly the "lignin barrier". They also use a multi-enzyme system including so-called "feedback" type enzymes allowing for simultaneous degradation of lignin and carbohydrates. The multi-enzymes including laccase support the proposed route by explaining how the high molecular weight enzymes can function in the wood complex. These enzymes may function separately or cooperate each other. In addition, veratryl alcohol oxidase, cellobiose dehydrogenase, arylalcohol dehydrogenase, and particularly low molecular mediators and radicals have an important role in wood biodegradation. However, the possibility of other mechanism as well as other enzymes, as operating as feedback systems in the process of wood degradation, could not be excluded.

• Journal of Microbiology and Biotechnology
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• v.24 no.4
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• pp.475-482
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• 2014

The metabolic pathway of eugenol degradation by thermophilic Geobacillus sp. AY 946034 strain was analyzed based on the lack of data about eugenol degradation by thermophiles. TLC, GC-MS, and biotransformation with resting cells showed that eugenol was oxidized through coniferyl alcohol, and ferulic and vanillic acids to protocatechuic acid before the aromatic ring was cleaved. The cell-free extract of Geobacillus sp. AY 946034 strain grown on eugenol showed a high activity of eugenol hydroxylase, feruloyl-CoA synthetase, vanillate-O-demethylase, and protocatechuate 3,4-dioxygenase. The key enzyme, protocatechuate 3,4-dioxygenase, which plays a crucial role in the degradation of various aromatic compounds, was purified 135-fold to homogeneity with a 34% overall recovery from Geobacillus sp. AY 946034. The relative molecular mass of the native enzyme was about $450{\pm}10$ kDa and was composed of the non-identical subunits. The pH and temperature optima for enzyme activity were 8 and $60^{\circ}C$, respectively. The half-life of protocatechuate 3,4-dioxygenase at the optimum temperature was 50 min.

• The Korean Journal of Mycology
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• v.14 no.3
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• pp.189-194
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• 1986

The aim of this study was to investigate physiological chracteristics of Lentinus edodes in Korea. We tried to detect properties of the several wood-degradative enzymes and investigate patterns of the enzyme production. A specific carbon source was used in the enzyme induction media for each enzymes, and the crude extract was used for the enzyme solution. With these enzyme solution, we investigated optimum temperature and pH conditions of their reactions. Moreover we investigated transition patterns of the enzyme production of the several wood-degrad­ative enzmes from Complex and Saw dust media for the purpose of studying the mechanisms of the wood component degradation by this fungus. It was assumed that the order of the wood com­ponent degradation was cellulose, xylan, and then pectic substances, and that the synergistic effects of these substances also influenced the degradation of wood components.

• Korean Journal of Food Science and Technology
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• v.22 no.5
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• pp.569-574
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• 1990

The influence of NaCl and pH on degradation of chicken breast muscle myofibrillar proteins by porcine leukocyte lysosomal proteinases was investigated. The degradation reactions were carried out at $38^{\circ}C$ for 24hours under different conditions. The degradation of myofibrillar proteins by leukocyte lysosomal enzymes at various pH values was limited to partial hydrolysis. Reactions at higher pH values resulted in lower molecular weight degradation products while reactions at lower pH resulted in higher molecular weight degradation products. When NaCl was added into the reaction mixture, enzyme activities of degradation were increased at all pH values studied, as evidenced by NPN-analysis and SDS-PAGE. More severe degradation was observed with higher salt concentration. The concentration of 0.5M NaCl in the reaction mixture gave more degradation of myosin heavy chain by enzyme than that of 0.1M NaCl.

• Journal of Microbiology and Biotechnology
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• v.11 no.6
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• pp.928-933
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• 2001

Approximately 0.1 mg/ml of polyvinyl alcohol (PVA) was degraded by the growing cell, Brevibacillus laterospours, for 30 h, and 0.2 mg/ml of PVA was degraded by the cell-free extract that was isolated from Brevibacillus laterosporus. Approximately $0.29{\mu}g$/ml of acetic acid was produced from PVA by using the cell-free extract as a catalyst for 40 min. $V_{max}\;and\;K_m$ value of purified PAV-degradation enzyme was 3.75g/l and 2.75 g/l/min in reaction with EDTA and 3.99 g/l and 2.98 g/l/min in reaction without EDTA, respectively. Molecular weight of the purified enzyme determined by SDS-PAGE was 63,000 Da. Alcohol dehydrogenase and aldehyde dehydrogenase activities were qualitatively detected on a native acrylamide gel by an active staining method, indicating the existence of the metabolic pathway to use PVA as a substrate.

• Parasites, Hosts and Diseases
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• v.40 no.2
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• pp.93-99
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• 2002

The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (slgA), IgG, and IgM. It also degraded $interleukin-1{\alpha}$ ($IL-l{\alpha}$) and $IL-l{\beta}$. Its activity was not inhibited by endogenous protease inhibitors, such as ${\alpha}$2-macroglobulin, ${\alpha}l-trypsin$ inhibitor, and ${\alpha}2-antiplasmin$. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthanoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

• Membrane Journal
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• v.19 no.1
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• pp.72-82
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• 2009

A mathematical model was written for simulating the removal of phenol from wastewater in enzyme-loaded membrane reactor (EMR). The numerical simulation program was developed so as to predict the degradation of phenol through an EMR. Numerical model proves to be effective in searching for optimal operating conditions and creating an optimal microenvironment for the biocatalyst in order to optimize productivity. In this study, several dimensionless parameters such as Thiele Modulus (${\phi}^2$, dimensionless Michaelis-Menten constant ($\xi$), Peclet number (Pe) were introduced to simplify their effects on system efficiency. In particular, the study of phenol conversion at different feed compositions shows that low phenol concentrations and high Thiele Modulus values lead to higher reactant degradation.

• Food Science and Preservation
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• v.3 no.1
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• pp.93-104
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• 1996

The cell wall components of fruit include cellulose. hemicellulose, pectin, glycoprotein etc., and the cell wall composition differs according to the kind of fruit. Fruit softening occurs as a result of a change in the cell wall polysaccharides : the middle lamella which links primary cell walls is composed of pectin. and primary cell walls are decomposed by a solution of middle lamella caused due to a result of pectin degradation by pectin degrading enzymes during ripening and softening, During fruit ripening and softening, contents of arabinose and galactose among non-cellulosic neutral sugars are notably decreased, and this occurs as a result of the degradation of pectin during fruit repening and softening since they are side-chained with pectin in the form of arabinogalactan and galactan Enzymes involved in the degradation of the cell wall include polygalacturonase, cellulose, pectinmethylesterase, glycosidase, etc., and various studies have been done on the change in enzyme activities during the ripening and softning of fruit. Among cell wall-degrading enzymes, polygalacturonase has the greatest effect on fruit softening, and its activity Increases during the maturating and softening of fruit. This softening leads to the textural change of fruit as a result of the degradation of cell wall polysaccharides by a cell wall degrading enzyme which exists in fruit.